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In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
They can also be converted into glucose. [4] This glucose can then be converted to triglycerides and stored in fat cells. [5] Proteins can be broken down by enzymes known as peptidases or can break down as a result of denaturation. Proteins can denature in environmental conditions the protein is not made for. [6]
The synthesis of a new peptide chain using the ribosome is very slow; the ribosome can even be stalled when it encounters a rare codon, a codon found at low concentrations in the cell. [6] The slow synthesis rate and any such pauses provide an individual protein domain with the necessary time to become folded before the production of subsequent ...
Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein.
Within these organisms are macromolecules (proteins and nucleic acids) which form the three-dimensional structures essential to their enzymatic activity. [2] Above the native temperature of the organism, thermal energy may cause the unfolding and denaturation, as the heat can disrupt the intramolecular bonds in the tertiary and quaternary ...
The chaperone-mediated autophagy (CMA) protein quality assurance by digesting oxidized and altered proteins under stressful circumstances and supplying amino acids through protein denaturation. [39] Autophagy is the primary intrinsic degradative system for peptides, fats, carbohydrates, and other cellular structures.
Biotin - Avidin can bind up to four molecules of biotin simultaneously with a high degree of affinity and specificity. Avidin is a tetrameric biotin-binding protein produced in the oviducts of birds, reptiles and amphibians and deposited in the whites of their eggs. Dimeric members of the avidin family are also found in some bacteria. [1]
For example, extremes of pH or temperature usually cause denaturation of all protein structure, but this is a non-specific effect. Similarly, some non-specific chemical treatments destroy protein structure: for example, heating in concentrated hydrochloric acid will hydrolyse the peptide bonds holding proteins together, releasing free amino acids.